NAMA_GEOKA
ID NAMA_GEOKA Reviewed; 340 AA.
AC Q5KXG9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NADPH dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01614};
DE EC=1.6.99.1 {ECO:0000255|HAMAP-Rule:MF_01614};
GN Name=namA {ECO:0000255|HAMAP-Rule:MF_01614}; OrderedLocusNames=GK2332;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
CC -!- FUNCTION: Catalyzes the reduction of the double bond of an array of
CC alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro
CC group of nitroester and nitroaromatic compounds. It could have a role
CC in detoxification processes. {ECO:0000255|HAMAP-Rule:MF_01614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01614};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01614};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01614}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. NamA subfamily. {ECO:0000255|HAMAP-Rule:MF_01614}.
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DR EMBL; BA000043; BAD76617.1; -; Genomic_DNA.
DR RefSeq; WP_011231814.1; NC_006510.1.
DR PDB; 3GR7; X-ray; 2.30 A; A/B=1-340.
DR PDB; 3GR8; X-ray; 2.50 A; A/B=1-340.
DR PDBsum; 3GR7; -.
DR PDBsum; 3GR8; -.
DR AlphaFoldDB; Q5KXG9; -.
DR SMR; Q5KXG9; -.
DR STRING; 235909.GK2332; -.
DR EnsemblBacteria; BAD76617; BAD76617; GK2332.
DR KEGG; gka:GK2332; -.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_2_1_9; -.
DR OMA; NQRRDQY; -.
DR EvolutionaryTrace; Q5KXG9; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd02932; OYE_YqiM_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01614; NamA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023663; NADPH_DH_bac.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR044152; YqjM-like.
DR PANTHER; PTHR43303; PTHR43303; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Flavoprotein; FMN; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..340
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216121"
FT BINDING 23..26
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 60
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 164..167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 307..308
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3GR8"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 136..156
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:3GR7"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3GR7"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:3GR7"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:3GR7"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3GR7"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:3GR7"
SQ SEQUENCE 340 AA; 37680 MW; A386C16F7EC573EE CRC64;
MNTMLFSPYT IRGLTLKNRI VMSPMCMYSC DTKDGAVRTW HKIHYPARAV GQVGLIIVEA
TGVTPQGRIS ERDLGIWSDD HIAGLRELVG LVKEHGAAIG IQLAHAGRKS QVPGEIIAPS
AVPFDDSSPT PKEMTKADIE ETVQAFQNGA RRAKEAGFDV IEIHAAHGYL INEFLSPLSN
RRQDEYGGSP ENRYRFLGEV IDAVREVWDG PLFVRISASD YHPDGLTAKD YVPYAKRMKE
QGVDLVDVSS GAIVPARMNV YPGYQVPFAE LIRREADIPT GAVGLITSGW QAEEILQNGR
ADLVFLGREL LRNPYWPYAA ARELGAKISA PVQYERGWRF
